“…It is therefore more interesting to insert a threonine into the peptide sequence and then dehydrate it, either once the peptide elongation is completed, or on a smaller sequence of the peptide which will then be inserted into the rest of the sequence. This dehydration reaction has been widely reported in the literature [ 74 , 75 ]. We report here some cases of dehydration to obtain dehydrobutyrine.…”
Lipopeptides are a class of compounds generally produced by microorganisms through hybrid biosynthetic pathways involving non-ribosomal peptide synthase and a polyketyl synthase. Cyanobacterial-produced laxaphycins are examples of this family of compounds that have expanded over the past three decades. These compounds benefit from technological advances helping in their synthesis and characterization, as well as in deciphering their biosynthesis. The present article attempts to summarize most of the articles that have been published on laxaphycins. The current knowledge on the ecological role of these complex sets of compounds will also be examined.
“…It is therefore more interesting to insert a threonine into the peptide sequence and then dehydrate it, either once the peptide elongation is completed, or on a smaller sequence of the peptide which will then be inserted into the rest of the sequence. This dehydration reaction has been widely reported in the literature [ 74 , 75 ]. We report here some cases of dehydration to obtain dehydrobutyrine.…”
Lipopeptides are a class of compounds generally produced by microorganisms through hybrid biosynthetic pathways involving non-ribosomal peptide synthase and a polyketyl synthase. Cyanobacterial-produced laxaphycins are examples of this family of compounds that have expanded over the past three decades. These compounds benefit from technological advances helping in their synthesis and characterization, as well as in deciphering their biosynthesis. The present article attempts to summarize most of the articles that have been published on laxaphycins. The current knowledge on the ecological role of these complex sets of compounds will also be examined.
Conventional methods for the construction of dehydroamino acids (ΔAAs), which are a unique class of nonproteinogenic amino acids, require the pre-installation of special amino acids. Herein, we report and demonstrate the practical utility of an N-chloropeptide strategy for the rapid construction of ΔAA-containing peptides. The electrophilic Nchlorination of peptide bonds is drastically accelerated by a catalytic amount of quinuclidine (ABCO), and the subsequent β-elimination of N-chloroamide efficiently provides ΔAAcontaining peptides in high yield. The strategy enables, for the first time, the construction of a wide variety of ΔAA residues in peptides without any pre-functionalized side chains and facilitates the late-stage installation of ΔAA motifs into already-constructed oligopeptides, including a medicinally important macrocyclic peptide.
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